Rigid control of synthesis of collagen types I and III by cells in culture Academic Article uri icon

Overview

MeSH Major

  • Braces
  • Exercise Therapy
  • Intervertebral Disc
  • Low Back Pain
  • Spinal Diseases

abstract

  • The composition of the triple helicoid collagen molecule is not hemogeneous. Type I collagen, composed of two α (I) chains and one α (II) chain, forms densely packed collagen fibrils as usually seen in the electronmicrographs; Type III collagen, composed of three α 1/III/ chains exists mainly in reticulin. The ratio of type I to Type III varies in different tissues. In more pliable tissues (skin, intestine, lungs) the ratio of Type I to Type III is 2-3 to 1. Rigid tissues as tendon and bones contain only Type I collagen. In pathological changes with sclerotic induration (arteriosclerosis, pulmonary fibrosis) Type I collagen is increased, in granulation tissue sections decreased. The results of the present experiments provide evidence that the cells of NB-6 line ( a diploid fibroblast cell line from newborn rabbit lung) produced in vitro collagen with a standard ratio of Type I to Type III, independent of the growth rate measured by 3H thymidine incorporation into DNA. The NB-6 cells synthesized Type I and Type III collagen in a ratio of 1.94 (66% Type I collagen and 34% Type III collagen). This ratio was maintained unchanged throughout 20 subpopulations and at different cultivation times of the cells. Detailed data of the analytical process based on chromatographic isolation of cyanogen bromide peptides followed by electrophoretic separation of 3H- and 14 C-labelled proline and hydroxyproline are included. (Romhanyi - Pecs)

publication date

  • December 1977

Research

keywords

  • Academic Article

Additional Document Info

start page

  • 152

end page

  • 4

volume

  • 268

number

  • 5616